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Volumn 78, Issue 6, 2010, Pages 1408-1422

Mapping of ligand-binding covities in proteins

Author keywords

Alignment independent; Binding sites; Bioinformatics; Drug design; Medicinal chemistry; PCA clustering tree; Physicochemical properties; Principal component analysis; Protein cavity comparison; Screen

Indexed keywords

SERINE PROTEINASE;

EID: 77951210909     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22655     Document Type: Article
Times cited : (35)

References (78)
  • 1
    • 44949110143 scopus 로고    scopus 로고
    • Method for comparing the structures of protein ligand-binding sites and application for predicting protein-drug interactions
    • DOI 10.1002/prot.21933
    • Minai R, Matsuo Y, Onuki H, Hirota H. Method for comparing the structures of protein ligand-binding sites and application for predicting protein-drug interactions. Proteins 2008;72:367-381. (Pubitemid 351809174)
    • (2008) Proteins: Structure, Function and Genetics , vol.72 , Issue.1 , pp. 367-381
    • Minai, R.1    Matsuo, Y.2    Onuki, H.3    Hirota, H.4
  • 2
    • 29444457054 scopus 로고    scopus 로고
    • Fold independent structural comparisons of protein-ligand binding sites for exploring functional relationships
    • Gold ND, Jackson RM. Fold independent structural comparisons of protein-ligand binding sites for exploring functional relationships. J Mol Biol 2006;355:1112-1124.
    • (2006) J Mol Biol , vol.355 , pp. 1112-1124
    • Gold, N.D.1    Jackson, R.M.2
  • 3
    • 0030724039 scopus 로고    scopus 로고
    • TESS: A geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases, Application to enzyme active sites
    • Wallace AC, Borkakoti N, Thornton JM. TESS: A geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases, Application to enzyme active sites. Protein Sci 1997;6:2308-2323.
    • (1997) Protein Sci , vol.6 , pp. 2308-2323
    • Wallace, A.C.1    Borkakoti, N.2    Thornton, J.M.3
  • 4
    • 0037375799 scopus 로고    scopus 로고
    • Efficient identification of side-chain patterns using a multidimensional index tree
    • Hameiryck T. Efficient identification of side-chain patterns using a multidimensional index tree. Proteins 2003;51:96-108.
    • (2003) Proteins , vol.51 , pp. 96-108
    • Hameiryck, T.1
  • 5
    • 0027967593 scopus 로고
    • A graph-theoretic approach to the identification of three-dimensional patterns of amino acid side-chains in protein structures
    • DOI 10.1006/jmbi.1994.1657
    • Artymiuk PJ, Poirrette AR, Grindley HM, Rice DW, Willett P. A graph-theoretic approach to the identification of 3-dimentional patterns of amino-acid side-chains in protein structures. J Mol Biol 1994;243:327-344. (Pubitemid 24331985)
    • (1994) Journal of Molecular Biology , vol.243 , Issue.2 , pp. 327-344
    • Artymiuk, P.J.1    Poirrette, A.R.2    Grindley, H.M.3    Rice, D.W.4    Willett, P.5
  • 6
    • 0033613813 scopus 로고    scopus 로고
    • Recognition of spatial motifs in protein structures
    • DOI 10.1006/jmbi.1998.2393
    • Kleywegt GJ. Recognition of spatial motifs in protein structures. J Mol Biol 1999;285:1887-1897. (Pubitemid 29060478)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1887-1897
    • Kleywegt, G.J.1
  • 8
    • 0036406643 scopus 로고    scopus 로고
    • A new method to detect related function among proteins independent of sequence and fold homology
    • DOI 10.1016/S0022-2836(02)00811-2
    • Schmitt S, Kuhn D, Klebe G. A new method to detect related function among proteins independent of sequence and fold homology. J Mol Biol 2002;323:387-406. (Pubitemid 35283699)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.2 , pp. 387-406
    • Schmitt, S.1    Kuhn, D.2    Klebe, G.3
  • 9
    • 33744935012 scopus 로고    scopus 로고
    • From the similarity analysis of protein cavities to the functional classification of protein families using cavbase
    • DOI 10.1016/j.jmb.2006.04.024, PII S0022283606004724
    • Kuhn D, Weskamp N, Schmitt S, Hullermeier E, Klebe G. From the similarity analysis of protein cavities to the functional classification of protein families using Cavbase. J Mol Biol 2006;359:1023-1044. (Pubitemid 43842050)
    • (2006) Journal of Molecular Biology , vol.359 , Issue.4 , pp. 1023-1044
    • Kuhn, D.1    Weskamp, N.2    Schmitt, S.3    Hullermeier, E.4    Klebe, G.5
  • 10
    • 2442614144 scopus 로고    scopus 로고
    • Recognition of functional sites in protein structures
    • DOI 10.1016/j.jmb.2004.04.012, PII S0022283604004139
    • Shulman-Peleg A, Nussiuov R, Wolfson HJ. Recognition of functional sites in protein structures. J Mol Biol 2004;339:607-633. (Pubitemid 38625909)
    • (2004) Journal of Molecular Biology , vol.339 , Issue.3 , pp. 607-633
    • Shulman-Peleg, A.1    Nussinov, R.2    Wolfson, H.J.3
  • 11
    • 0034018755 scopus 로고    scopus 로고
    • Mapping of protein surface cavities and prediction of enzyme class by a self-organizing neural network
    • 11.StahlM,TaroniC,SchneiderG. Mappingofproteinsurfacecavitiesandpredictionofenzymeclassbyaself- organizingneuralnetwork.ProteinEngDesSel2000;13:83-88.(Pubitemid30151038)
    • (2000) Protein Engineering , vol.13 , Issue.2 , pp. 83-88
    • Stahl, M.1    Taroni, C.2    Schneider, G.3
  • 12
    • 33646757492 scopus 로고    scopus 로고
    • On the nature of cavities on protein surfaces: Application to the identification of drug-binding sites
    • DOI 10.1002/prot.20897
    • Naval M, Honig B. On the nature of cavities on protein surfaces: Application to the identification of drug-binding sites. Proteins 2006;63:892-906. (Pubitemid 43765141)
    • (2006) Proteins: Structure, Function and Genetics , vol.63 , Issue.4 , pp. 892-906
    • Nayal, M.1    Honig, B.2
  • 13
    • 42449144314 scopus 로고    scopus 로고
    • Large scale analysis of protein-binding cavities using self-organizing maps and wavelet-based surface patches to describe functional properties, selectivity discrimination, and putative cross-reactivity
    • DOI 10.1002/prot.21823
    • Kupas K, Ultsch A, Klebe G. Large scale analysis of protein-binding cavities using self-organizing maps and wavelet-based surface patches to describe functional properties, selectivity discrimination, and putative cross-reactivity. Proteins 2008;71:1288-1306. (Pubitemid 351564053)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.3 , pp. 1288-1306
    • Kupas, K.1    Ultsch, A.2    Klebe, G.3
  • 14
    • 0031687653 scopus 로고    scopus 로고
    • Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design
    • LiangJ,EdelsbrunnerH,WoodwardC.Anatomyofproteinpocketsandcavities: measurementofbindingsitegeometryandimplicationsforliganddesign.ProteinSci1998;7: 1884-1897.(Pubitemid28432430)
    • (1998) Protein Science , vol.7 , Issue.9 , pp. 1884-1897
    • Liang, J.1    Edelsbrunner, H.2    Woodward, C.3
  • 15
    • 0041989751 scopus 로고    scopus 로고
    • CASTp: Computed Atlas of Surface Topography of proteins
    • DOI 10.1093/nar/gkg512
    • Binkowski TA, Naghibzadeh S, Liang J. CASTp: Computed atlas of surface topography of proteins. Nucleic Acids Res 2003;31:3352-3355. (Pubitemid 37442157)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3352-3355
    • Binkowski, T.A.1    Naghibzadeh, S.2    Liang, J.3
  • 16
    • 3242883091 scopus 로고    scopus 로고
    • PvSOAR: Detecting similar surface patterns of pocket and void surfaces of amino acid residues on proteins
    • DOI 10.1093/nar/gkh390
    • Binkowski TA, Freeman P, Liang J. pvSOAR: Detecting similar surface patterns of pocket and void surfaces of amino acid residues on proteins. Nucleic Acids Res 2004;32:W555-W558. (Pubitemid 38997395)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS
    • Binkowski, T.A.1    Freeman, P.2    Liang, J.3
  • 17
    • 58349103124 scopus 로고    scopus 로고
    • Protein functional surfaces: Global shape matching and local spatial alignments of ligand binding sites
    • Binkowski TA, Joachimiak A. Protein functional surfaces: global shape matching and local spatial alignments of ligand binding sites. BMC Struct Biol 2008;8:23.
    • (2008) BMC Struct Biol , vol.8 , pp. 23
    • Binkowski, T.A.1    Joachimiak, A.2
  • 19
    • 34447645811 scopus 로고    scopus 로고
    • A robust and efficient algorithm for the shape description of protein structures and its application in predicting ligand binding sites
    • DOI 10.1186/1471-2105-8-S4-S9
    • Xie L, Bourne PE. A robust and efficient algorithm for the shape description of protein structures and its application in predicting ligand binding sites. BMC Bioinf 2007;8:S9. (Pubitemid 351833828)
    • (2007) BMC Bioinformatics , vol.8 , Issue.SUPPL. 4
    • Xie, L.1    Bourne, P.E.2
  • 21
    • 20444450051 scopus 로고    scopus 로고
    • Predicting protein function from sequence and structural data
    • DOI 10.1016/j.sbi.2005.04.003, PII S0959440X05000825
    • Watson JD, Laskowski RA, Thornton JM. Predicting protein function from sequence and structural data. Curr Opin Struct Biol 2005;15:275-284. (Pubitemid 40826446)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.3 SPEC. ISS , pp. 275-284
    • Watson, J.D.1    Laskowski, R.A.2    Thornton, J.M.3
  • 22
    • 30144443247 scopus 로고    scopus 로고
    • Similarity networks of protein binding sites
    • Zhang ZD, Grigorov MG. Similarity networks of protein binding sites. Proteins 2006;62:470-478.
    • (2006) Proteins , vol.62 , pp. 470-478
    • Zhang, Z.D.1    Grigorov, M.G.2
  • 23
    • 0017429069 scopus 로고
    • Areas, volumes, packing, and protein-structure
    • Richards FM. Areas, volumes, packing, and protein-structure. Ann Rev Biophys Bioeng 1977;6:151-176.
    • (1977) Ann Rev Biophys Bioeng , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 25
    • 0028881975 scopus 로고
    • Surfnet-A program for visualizing molecular-surfaces, cavities and intermolecular interactions
    • Laskowski RA. Surfnet-A program for visualizing molecular-surfaces, cavities and intermolecular interactions. J Mol Graph 1995; 13: 323-330.
    • (1995) J Mol Graph , vol.13 , pp. 323-330
    • Laskowski, R.A.1
  • 26
    • 0041842509 scopus 로고    scopus 로고
    • Identification of protein biochemical functions by similarity search using the molecular surface database eF-site
    • DOI 10.1110/ps.0368703
    • Kinoshita K, Nakamura H. Identification of protein biochemical functions by similarity search using the molecular surface database eF-site. Protein Sci 2003;12:1589-1595. (Pubitemid 36910039)
    • (2003) Protein Science , vol.12 , Issue.8 , pp. 1589-1595
    • Kinoshita, K.1    Nakamura, H.2
  • 27
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleicacids
    • Connolly ML. Solvent-accessible surfaces of proteins and nucleicacids. Science 1983;221:709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 29
    • 34547341277 scopus 로고    scopus 로고
    • PocketPicker: Analysis of ligand binding-sites with shape descriptors
    • Weisel M, Proschak E, Schneider G. PocketPicker: analysis of ligand binding-sites with shape descriptors. Chem Cent J 2007;1:7.
    • (2007) Chem Cent J , vol.1 , pp. 7
    • Weisel, M.1    Proschak, E.2    Schneider, G.3
  • 30
    • 0026319199 scopus 로고
    • Protein folding and associationinsights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. Protein folding and associationinsights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 32
    • 50849126111 scopus 로고    scopus 로고
    • Rapid comparison of properties on protein surface
    • Sael L, La D, Li B, Rustamov R, Kihara D. Rapid comparison of properties on protein surface. Proteins 2008;73:1-10.
    • (2008) Proteins , vol.73 , pp. 1-10
    • Sael, L.1    La, D.2    Li, B.3    Rustamov, R.4    Kihara, D.5
  • 33
    • 51349090017 scopus 로고    scopus 로고
    • Fast protein tertiary structure retrieval based on global surface shape similarity
    • Sael L, Li B, La D, Fang Y, Ramani K, Rustamov R, Kihara D. Fast protein tertiary structure retrieval based on global surface shape similarity. Proteins 2008;72:1259-1273.
    • (2008) Proteins , vol.72 , pp. 1259-1273
    • Sael, L.1    Li, B.2    La, D.3    Fang, Y.4    Ramani, K.5    Rustamov, R.6    Kihara, D.7
  • 35
    • 34249291647 scopus 로고    scopus 로고
    • Advances in exploration of machine learning methods for predicting functional class and interaction profiles of proteins and peptides irrespective of sequence homology
    • Cui JA, Han LY, Lin HH, Tang ZQ, Ji ZL, Cao ZW, Li YX, Chen YZ. Advances in exploration of machine learning methods for predicting functional class and interaction profiles of proteins and peptides irrespective of sequence homology. Curr Bioinf 2007;2:95-112.
    • (2007) Curr Bioinf , vol.2 , pp. 95-112
    • Cui, J.A.1    Han, L.Y.2    Lin, H.H.3    Tang, Z.Q.4    Ji, Z.L.5    Cao, Z.W.6    Li, Y.X.7    Chen, Y.Z.8
  • 36
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L, Sander C. Mapping the protein universe. Science 1996; 273:595-602.
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sander, C.2
  • 38
    • 54749109580 scopus 로고    scopus 로고
    • How to measure the similarity between protein ligand-binding sites?
    • Kellenberger E, Schalon C, Rognan D. How to measure the similarity between protein ligand-binding sites? Curr Comput-Aided Drug Des 2008;4:209-220.
    • (2008) Curr Comput-Aided Drug des , vol.4 , pp. 209-220
    • Kellenberger, E.1    Schalon, C.2    Rognan, D.3
  • 39
    • 0002068233 scopus 로고    scopus 로고
    • ChemGPS: A chemical space navigation tool
    • Oprea TI, Gottfries J. ChemGPS: a chemical space navigation tool. Rat Appr Drug Des 2001:437-446.
    • (2001) Rat Appr Drug des , pp. 437-446
    • Oprea, T.I.1    Gottfries, J.2
  • 40
    • 77951232051 scopus 로고    scopus 로고
    • ChemGPSNP-tuned for navigation in biologically relevant chemical space
    • Larsson J, Gottfries J, Muresan S, Bohlin L, Backlund A. ChemGPSNP-tuned for navigation in biologically relevant chemical space. Planta Medica 2006;72:1020-1021.
    • (2006) Planta Medica , vol.72 , pp. 1020-1021
    • Larsson, J.1    Gottfries, J.2    Muresan, S.3    Bohlin, L.4    Backlund, A.5
  • 41
    • 30844443282 scopus 로고    scopus 로고
    • Molecular similarity and diversity in chemoinformatics: From theory to applications
    • Maldonado AG, Doucet JP, Petitjean M, Fan BT. Molecular similarity and diversity in chemoinformatics: from theory to applications. Mol Diversity 2006;10:39-79.
    • (2006) Mol Diversity , vol.10 , pp. 39-79
    • Maldonado, A.G.1    Doucet, J.P.2    Petitjean, M.3    Fan, B.T.4
  • 42
    • 33644861784 scopus 로고    scopus 로고
    • Diversity in medicinal chemistry space
    • Gorse AD. Diversity in medicinal chemistry space. Curr Top Med Chem 2006;6:3-18.
    • (2006) Curr Top Med Chem , vol.6 , pp. 3-18
    • Gorse, A.D.1
  • 43
    • 33845550710 scopus 로고
    • Multivariate quantitative structure activity relationships (QSAR)-conditions for their applicability
    • Wold S, Dunn WJ. Multivariate quantitative structure activity relationships (QSAR)-conditions for their applicability. J Chem Inf Comput Sci 1983;23:6-13.
    • (1983) J Chem Inf Comput Sci , vol.23 , pp. 6-13
    • Wold, S.1    Dunn, W.J.2
  • 44
    • 33751176669 scopus 로고    scopus 로고
    • Quantitative structure-pharmacokinetic/pharmacody-namic relationships
    • Mager DE. Quantitative structure-pharmacokinetic/pharmacody-namic relationships. Adv Drug Delivery Rev 2006;58:1326-1356.
    • (2006) Adv Drug Delivery Rev , vol.58 , pp. 1326-1356
    • Mager, D.E.1
  • 45
    • 67649100477 scopus 로고    scopus 로고
    • A chemogenomics view on proteinligand spaces
    • Strombergsson H, Kleywegt GJ. A chemogenomics view on proteinligand spaces. BMC Bioinf 2009;10.
    • (2009) BMC Bioinf , pp. 10
    • Strombergsson, H.1    Kleywegt, G.J.2
  • 47
    • 57649221999 scopus 로고    scopus 로고
    • Quantitative protein descriptors for secondary structure characterization and protein classification
    • Lindstrom A, Pettersson F, Linusson A. Quantitative protein descriptors for secondary structure characterization and protein classification. Chemom Intell Lab Syst 2009;95:74-85.
    • (2009) Chemom Intell Lab Syst , vol.95 , pp. 74-85
    • Lindstrom, A.1    Pettersson, F.2    Linusson, A.3
  • 48
    • 0037030707 scopus 로고    scopus 로고
    • Structural classification of protein kinases using 3D molecular interaction field analysis of their ligand binding sites: Target family landscapes
    • Naumann T, Matter H. Structural classification of protein kinases using 3D molecular interaction field analysis of their ligand binding sites: Target family landscapes. J Med Chem 2002;45:2366-2378.
    • (2002) J Med Chem , vol.45 , pp. 2366-2378
    • Naumann, T.1    Matter, H.2
  • 49
    • 0028961335 scopus 로고
    • SCOP-a structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. SCOP-a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995;247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 50
    • 2542530042 scopus 로고    scopus 로고
    • The PDBbind database: Collection of binding affinities for protein-ligand complexes with known three-dimensional structures
    • Wang R, Fang X, Lu Y, Wang S. The PDBbind database: collection of binding affinities for protein-ligand complexes with known three-dimensional structures. J Med Chem 2004;47:2977-2980.
    • (2004) J Med Chem , vol.47 , pp. 2977-2980
    • Wang, R.1    Fang, X.2    Lu, Y.3    Wang, S.4
  • 51
    • 20444422149 scopus 로고    scopus 로고
    • The PDBbind database: Methodologies and updates
    • Wang R, Fang X, Lu Y, Yang C-Y, Wang S. The PDBbind database: methodologies and updates. J Med Chem 2005;48:4111-4119.
    • (2005) J Med Chem , vol.48 , pp. 4111-4119
    • Wang, R.1    Fang, X.2    Lu, Y.3    Yang, C.-Y.4    Wang, S.5
  • 52
    • 77951219977 scopus 로고    scopus 로고
    • The Richardson Laboratory. Reduce. 3.03. Duke University: Durham NC.
    • The Richardson Laboratory. Reduce. 3.03. Duke University: Durham NC.
  • 53
    • 84860134058 scopus 로고    scopus 로고
    • Accessed on 2009-08-18.
    • RCSB Protein data Bank. http://www.rcsb.org. Accessed on 2009-08-18.
    • RCSB Protein Data Bank
  • 56
    • 0004313709 scopus 로고    scopus 로고
    • Chemical Computing Group Inc. MOE Version 2008.10. Sherbrooke St. W, Montreal, Quebec: Chemical Computing Group Inc
    • Chemical Computing Group Inc. MOE (Molecular Operating Environment). Version 2008.10. Sherbrooke St. W, Montreal, Quebec: Chemical Computing Group Inc; 2008.
    • (2008) Molecular Operating Environment
  • 59
    • 84860152432 scopus 로고    scopus 로고
    • Umbio. Evince. 2.2.2. Umeå, Sweden.
    • Umbio. Evince. 2.2.2. Umeå, Sweden.
  • 60
    • 85164278893 scopus 로고
    • Partial least squares analysis with cross-validation for the two-class problem: A monte carlo study
    • Stahle L, Wold S. Partial least squares analysis with cross-validation for the two-class problem: a monte carlo study. J Chemom 1987;1; 185-196.
    • (1987) J Chemom , vol.1 , pp. 185-196
    • Stahle, L.1    Wold, S.2
  • 62
    • 0023375195 scopus 로고
    • The neighbor-joining method-a new method for reconstructing phylogenetic trees
    • Saitou N, Nei M. The neighbor-joining method-a new method for reconstructing phylogenetic trees. Mol Biol Evol 1987;4:406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 64
    • 84860167166 scopus 로고    scopus 로고
    • Accessed on 2008-08-106
    • Lloyd A. Clusta1W2. 1997. http://www.ebi.ac.uk/Tools/clust.alw2/index. html. Accessed on 2008-08-106
    • (1997) Clusta1W2
    • Lloyd, A.1
  • 65
    • 77951224605 scopus 로고    scopus 로고
    • Openeye scientific software Inc. Santa Fe, NM: Openeye scientific software Inc
    • Openeye scientific software Inc. ROCS. 2.2. Santa Fe, NM: Openeye scientific software Inc; 2006.
    • (2006) ROCS. 2.2
  • 66
    • 34250779428 scopus 로고    scopus 로고
    • ChemGPS-NP: Tuned for navigation in biologically relevant chemical space
    • Larsson J, Gottfries J, Muresan S, Backlund A, ChemGPS-NP: tuned for navigation in biologically relevant chemical space. J Nat Prod 2007;70:789-794.
    • (2007) J Nat Prod , vol.70 , pp. 789-794
    • Larsson, J.1    Gottfries, J.2    Muresan, S.3    Backlund, A.4
  • 67
    • 46849089254 scopus 로고    scopus 로고
    • Recent developments in fragment-based drug discovery
    • Congreve M, Chessari G, Tisi D, Woodhead AJ. Recent developments in fragment-based drug discovery. J Med Chem 2008;51: 3661-3680.
    • (2008) J Med Chem , vol.51 , pp. 3661-3680
    • Congreve, M.1    Chessari, G.2    Tisi, D.3    Woodhead, A.J.4
  • 71
    • 41349093325 scopus 로고    scopus 로고
    • Multiple protein structures and multiple ligands: Effects on the apparent goodness of virtual screening results
    • Sheridan RP, McGaughey GB, Cornell WD. Multiple protein structures and multiple ligands: effects on the apparent goodness of virtual screening results. J Comput Aided Mol Des 2008:22:257-265.
    • (2008) J Comput Aided Mol des , vol.22 , pp. 257-265
    • Sheridan, R.P.1    McGaughey, G.B.2    Cornell, W.D.3
  • 73
    • 51649083818 scopus 로고    scopus 로고
    • Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics
    • Xu YC, Colletier JP, Weik M, Jiang HL, Moult J, Silman I, Sussman JL. Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics. Biophys J 2008;95: 2500-2511.
    • (2008) Biophys J , vol.95 , pp. 2500-2511
    • Xu, Y.C.1    Colletier, J.P.2    Weik, M.3    Jiang, H.L.4    Moult, J.5    Silman, I.6    Sussman, J.L.7
  • 74
    • 0028172534 scopus 로고
    • The immunoglobulin fold-structural classification, sequence patterns and common core
    • Bork P, Holm L, Sander C. The immunoglobulin fold-structural classification, sequence patterns and common core. J Mol Biol 1994;242:309-320.
    • (1994) J Mol Biol , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 76
    • 0032512806 scopus 로고    scopus 로고
    • Contributions of orientation and hydrogen bonding to catalysis in Asn229 mutants of thymidylate synthase
    • Finer-Moore JS, Liu L, Birdsall DL, Brem R, Apfeld J, Santi DV, Stroud RM. Contributions of orientation and hydrogen bonding to catalysis in Asn229 mutants of thymidylate synthase. J Mol Biol 1998;276:113-129.
    • (1998) J Mol Biol , vol.276 , pp. 113-129
    • Finer-Moore, J.S.1    Liu, L.2    Birdsall, D.L.3    Brem, R.4    Apfeld, J.5    Santi, D.V.6    Stroud, R.M.7
  • 77
    • 0029923190 scopus 로고    scopus 로고
    • Partitioning roles of side chains in affinity, orientation, and catalysis with structures for mutant complexes: Aspargine-229 in thymidylate synthase
    • Finer-Moore JS, Liu L, Schafmeister CE, Birdsall DL, Mau T, Santi DV, Stroud RM. Partitioning roles of side chains in affinity, orientation, and catalysis with structures for mutant complexes: Aspargine-229 in thymidylate synthase. Biochemistry 1996;35:5125-5136.
    • (1996) Biochemistry , vol.35 , pp. 5125-5136
    • Finer-Moore, J.S.1    Liu, L.2    Schafmeister, C.E.3    Birdsall, D.L.4    Mau, T.5    Santi, D.V.6    Stroud, R.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.